Myosin chaperones.
Myosin chaperones.
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DOI:
10.1016/j.sbi.2013.11.002
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发表时间:
2014-04
影响因子:
6.8
通讯作者:
Clausen T
中科院分区:
文献类型:
--
作者:
Hellerschmied D;Clausen T
UCS proteins comprise a diverse family of myosin chaperones. UCS chaperones differ in their substrate targeting, folding and activation mechanism. TPR-less UCS chaperones dimerize to control the myosin–actin interaction. TPR-containing UCS proteins compose multimeric assembly lines for myofilaments. Misregulation of UCS activity is linked to myopathies including heart diseases. The folding and assembly of myosin motor proteins is essential for most movement processes at the cellular, but also at the organism level. Importantly, myosins, which represent a very diverse family of proteins, require the activity of general and specialized folding factors to develop their full motor function. The activities of the myosin-specific UCS (UNC-45/Cro1/She4) chaperones range from assisting acto-myosin dependent transport processes to scaffolding multi-subunit chaperone complexes, which are required to assemble myofilaments. Recent structure–function studies revealed the structural organization of TPR (tetratricopeptide repeat)-containing and TPR-less UCS chaperones. The observed structural differences seem to reflect the specialized and remarkably versatile working mechanisms of myosin-directed chaperones, as will be discussed in this review.
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